Information on EC 1.1.1.326 - zerumbone synthase

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The expected taxonomic range for this enzyme is: Zingiber zerumbet

EC NUMBER
COMMENTARY hide
1.1.1.326
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RECOMMENDED NAME
GeneOntology No.
zerumbone synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
10-hydroxy-alpha-humulene + NAD+ = zerumbone + NADH + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
zerumbone biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
10-hydroxy-?-humulene:NAD+ oxidoreductase
The enzyme was cloned from shampoo ginger, Zingiber zerumbet.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene ZSD1
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
ZSD1 is a member of the short-chain dehydrogenase/reductase superfamily, SDR, and shares high identities with other plant SDRs involved in secondary metabolism, stress responses and phytosteroid biosynthesis
metabolism
ZSD1 is an alcohol dehydrogenase capable of catalyzing the final step of zerumbone biosynthesis, but ZSD1 is also be involved in other biological processes
physiological function
ZSD1 is involved in secondary metabolism, stress responses and phytosteroid biosynthesis
additional information
the enzyme contains an active site sequence 155Y-X-X-X-K159, Ser142 completes the Ser-Tyr-Lys triad responsible for the catalysis of ZSD1
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
10-hydroxy-alpha-humulene + NAD+
zerumbone + NADH + H+
show the reaction diagram
additional information
?
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the enzyme also converts borneol to camphor in vitro with Km and kcat values of 0.0228 mM and 4.1/s
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
10-hydroxy-alpha-humulene + NAD+
zerumbone + NADH + H+
show the reaction diagram
F1SWA0
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
ZSD1 contains an NAD+-binding motif TGxxxGxG
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.028 - 0.138
10-hydroxy-alpha-humulene
0.0161 - 0.121
NAD+
additional information
additional information
kinetics with borneol as substrate
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1 - 2.9
10-hydroxy-alpha-humulene
0.1 - 4.4
NAD+
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000007 - 0.000103
10-hydroxy-alpha-humulene
6389
0.0000008 - 0.000262
NAD+
7
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.63
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
contains an exceptionally high level of sesquiterpenoids with zerumbone
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28700
x * 28700, sequence calculation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 28700, sequence calculation
additional information
a 3D structure model of ZSD1 reveals a large, flexible substrate-binding pocket, molecular modeling, overview
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3)
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene ZSD1, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K159A
site-directed mutagenesis, inactive mutant
S142A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S144A
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
Y155A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pharmacology
zerumbone is a predominating potential multi-anticancer agent